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Malate is acted on by malate dehydrogenase to become oxaloacetate, producing a molecule of NADH. After that, oxaloacetate will be recycled to aspartate, as transaminases prefer these keto acids over the others. This recycling maintains the flow of nitrogen into the cell. Relationship of oxaloacetic acid, malic acid, and aspartic acid
The amino acid sequences of archaeal MDH are more similar to that of LDH than that of MDH of other organisms. This indicates that there is a possible evolutionary linkage between lactate dehydrogenase and malate dehydrogenase. [8] Each subunit of the malate dehydrogenase dimer has two distinct domains that vary in structure and functionality.
The reaction it catalyzes is: pyruvate + HCO − 3 + ATP → oxaloacetate + ADP + P. It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. PC contains a biotin prosthetic group [1] and is typically localized to the mitochondria in eukaryotes with exceptions to some fungal species such as Aspergillus nidulans which have a cytosolic PC.
Oxaloacetate + 2 H + + 2 e − → Malate-0.17 [10] While under standard conditions malate cannot reduce the more electronegative NAD +:NADH couple, in the cell the concentration of oxaloacetate is kept low enough that Malate dehydrogenase can reduce NAD + to NADH during the citric acid cycle. Fumarate + 2 H + + 2 e − → Succinate +0.03 [9]
1. CO 2 is fixed to produce a four-carbon molecule (malate or aspartate). 2. The molecule exits the cell and enters the bundle sheath cells. 3. It is then broken down into CO 2 and pyruvate. CO 2 enters the Calvin cycle to produce carbohydrates. 4. Pyruvate reenters the mesophyll cell, where it is reused to produce malate or aspartate.
In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction below (S)-malate + NAD + pyruvate + CO 2 + NADH. Thus, the two substrates of this enzyme are (S)-malate and NAD +, whereas its 3 products are pyruvate, CO 2, and NADH.
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Other glucogenic amino acids and all citric acid cycle intermediates (through conversion to oxaloacetate) can also function as substrates for gluconeogenesis. [9] Generally, human consumption of gluconeogenic substrates in food does not result in increased gluconeogenesis. [10] In ruminants, propionate is the principal gluconeogenic substrate.